ID A0A2S6NNN2_RHOGL Unreviewed; 518 AA.
AC A0A2S6NNN2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Sulfate adenylyltransferase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00062};
DE EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00062};
DE AltName: Full=ATP-sulfurylase large subunit {ECO:0000256|HAMAP-Rule:MF_00062};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00062};
DE Short=SAT {ECO:0000256|HAMAP-Rule:MF_00062};
GN Name=cysN {ECO:0000256|HAMAP-Rule:MF_00062};
GN ORFNames=CCS01_01735 {ECO:0000313|EMBL:PPQ39033.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ39033.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ39033.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ39033.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
CC -!- FUNCTION: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the
CC adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and
CC diphosphate, the first enzymatic step in sulfur assimilation pathway.
CC APS synthesis involves the formation of a high-energy phosphoric-
CC sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled
CC to ATP hydrolysis by CysD. {ECO:0000256|HAMAP-Rule:MF_00062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00062};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_00062}.
CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC {ECO:0000256|HAMAP-Rule:MF_00062}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. CysN/NodQ
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00062}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPQ39033.1}.
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DR EMBL; NHRY01000036; PPQ39033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6NNN2; -.
DR OrthoDB; 9804504at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000239724; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR CDD; cd04166; CysN_ATPS; 1.
DR CDD; cd03695; CysN_NodQ_II; 1.
DR CDD; cd04095; CysN_NoDQ_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
DR InterPro; IPR041757; CysN_GTP-bd.
DR InterPro; IPR044138; CysN_II.
DR InterPro; IPR044139; CysN_NoDQ_III.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011779; SO4_adenylTrfase_lsu.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR NCBIfam; TIGR02034; CysN; 1.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00062};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00062}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00062};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00062}; Reference proteome {ECO:0000313|Proteomes:UP000239724};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00062}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 471..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..290
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062"
FT BINDING 107..111
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062"
FT BINDING 162..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062"
SQ SEQUENCE 518 AA; 55782 MW; 01DC155E596F6742 CRC64;
MSVALADTAP LAEVAVREAS LLRFLTCGSV DDGKSTLLGR LLFDSHAVLD DQLAALDRDS
RKFSTHEGHR DFALLVDGLS AEREQGITID VAYRYFSTPK RSFIVADTPG HEQYTRNMAT
GASTAELAII LVDARKGILP QTRRHSFIVS MVGVRHVVLA VNKMDLMGFD QAVYDRIVAD
YTSAVVSLGF ETIVPIPMCA REGDNVAERS ERTPWYQGTP LLDYLESVDV GEAPDKAKRL
HLPVQWVNRP NLDFRGYAGT VSAGTAHVGD PVTVLPSLRH SSIARIVTAE GDLEAASVGQ
AVTLTLADEV DISRGDVIVH RSSVMQAHTA ITARLLWMGE APMRPGQSFI VKLGTMEANA
TVAKLRHAVD IHSFQNQPAD SLAMNGIGVV DLRFDKPLSA TIYGRDRTLG SFILIERMTN
QTVALGTVEA AAQRQANDNS RAQVVPRAVG AVAGRQRARF RALVGCRIAE AVMLALIVWL
LSGSGYLALA VAAVDAVLRP MAGRVAMLLG GRGNAVLS
//
